The Affiliated Hospital of Medical School, Ningbo University, Ningbo 315020, China; Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathphysiology, Medical School of Ningbo University, Ningbo 315211, China.
The Affiliated Hospital of Medical School, Ningbo University, Ningbo 315020, China; Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathphysiology, Medical School of Ningbo University, Ningbo 315211, China.
Gene. 2022 Jul 20;832:146562. doi: 10.1016/j.gene.2022.146562. Epub 2022 May 14.
Ubiquitination of substrates usually have two fates: one is degraded by 26S proteasome, and the other is non-degradative ubiquitination modification which is associated with cell cycle regulation, chromosome inactivation, protein transportation, tumorigenesis, achondroplasia, and neurological diseases. Cullin3 (CUL3), a scaffold protein, binding with the Bric-a-Brac-Tramtrack-Broad-complex (BTB) domain of substrates recognition adaptor and RING-finger protein 1 (RBX1) form ubiquitin ligases (E3). Based on the current researches, this review has summarized the functions and effects of CUL3-E3 ligases mediated non-degradative ubiquitination.
一种是被 26S 蛋白酶体降解，另一种是非降解性泛素化修饰，与细胞周期调控、染色体失活、蛋白质运输、肿瘤发生、软骨发育不全和神经退行性疾病有关。Cullin3（CUL3）是一种支架蛋白，与底物识别衔接子的 Bric-a-Brac-Tramtrack-Broad-complex（BTB）结构域和 RING-finger 蛋白 1（RBX1）结合形成泛素连接酶（E3）。基于目前的研究，本综述总结了 CUL3-E3 连接酶介导的非降解性泛素化的功能和作用。
